4jhr

An auto-inhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs

spinqualitylabelsall models 4jhr, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jhr is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GPSM2_MOUSE Plays an important role in spindle pole orientation (By similarity). Interacts and contributes to the functional activity of G(i) alpha proteins. Acts to stabilize the apical complex during neuroblast divisions. Publication Abstract from PubMed LGN plays essential roles in asymmetric cell divisions via its N-terminal TPR-motif-mediated binding to mInsc and NuMA. This scaffolding activity requires the release of the autoinhibited conformation of LGN by binding of Galphai to its C-terminal GoLoco (GL) motifs. The interaction between the GL and TPR motifs of LGN represents a distinct GL/target binding mode with an unknown mechanism. Here, we show that two consecutive GL motifs of LGN form a minimal TPR-motif-binding unit. GL12 and GL34 bind to TPR0-3 and TPR4-7, respectively. The crystal structure of a truncated LGN reveals that GL34 forms a pair of parallel alpha helices and binds to the concave surface of TPR4-7, thereby preventing LGN from binding to other targets. Importantly, the GLs bind to TPR motifs with a mode distinct from that observed in the GL/Galphai.GDP complexes. Our results also indicate that multiple and orphan GL motif proteins likely respond to G proteins with distinct mechanisms. An Autoinhibited Conformation of LGN Reveals a Distinct Interaction Mode between GoLoco Motifs and TPR Motifs.,Pan Z, Zhu J, Shang Y, Wei Z, Jia M, Xia C, Wen W, Wang W, Zhang M Structure. 2013 Jun 4;21(6):1007-17. doi: 10.1016/j.str.2013.04.005. Epub 2013, May 9. PMID:23665171 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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